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Protein

Short-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acads

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Introduces a double bond at position 2 in saturated acyl-CoAs of short chain length, i.e. less than 6 carbon atoms.1 Publication

Miscellaneous

A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.

Catalytic activityi

A short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.1 Publication

Cofactori

FAD2 PublicationsNote: Binds 1 FAD per subunit.2 Publications

Kineticsi

  1. KM=10.7 µM for butanoyl-CoA1 Publication
  2. KM=32.9 µM for pentanoyl-CoA1 Publication
  3. KM=285 µM for hexanoyl-CoA1 Publication
  1. Vmax=28.3 µmol/min/mg enzyme with butanoyl-CoA as substrate1 Publication
  2. Vmax=24.3 µmol/min/mg enzyme with pentanoyl-CoA as substrate1 Publication
  3. Vmax=8.5 µmol/min/mg enzyme with hexanoyl-CoA as substrate1 Publication

Pathwayi: mitochondrial fatty acid beta-oxidation

This protein is involved in the pathway mitochondrial fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway mitochondrial fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei161Substrate; via carbonyl oxygen1 Publication1
Binding sitei297FAD1 Publication1
Active sitei392Proton acceptor1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi152 – 161FAD1 Publication10
Nucleotide bindingi185 – 187FAD1 Publication3
Nucleotide bindingi365 – 369FAD1 Publication5
Nucleotide bindingi394 – 396FAD1 Publication3

GO - Molecular functioni

  • acyl-CoA dehydrogenase activity Source: RGD
  • butyryl-CoA dehydrogenase activity Source: RGD
  • fatty-acyl-CoA binding Source: RGD
  • flavin adenine dinucleotide binding Source: RGD

GO - Biological processi

  • butyrate catabolic process Source: RGD
  • fatty acid beta-oxidation Source: RGD
  • fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: RGD
  • protein homotetramerization Source: RGD
  • response to glucocorticoid Source: RGD
  • response to starvation Source: RGD

Keywordsi

Molecular functionOxidoreductase
Biological processFatty acid metabolism, Lipid metabolism
LigandFAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.3.8.1 5301
SABIO-RKP15651
UniPathwayiUPA00660

Names & Taxonomyi

Protein namesi
Recommended name:
Short-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.11 Publication)
Short name:
SCAD
Alternative name(s):
Butyryl-CoA dehydrogenase
Gene namesi
Name:Acads
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620514 Acads

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2176825

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 24Mitochondrion1 PublicationAdd BLAST24
ChainiPRO_000000050125 – 412Short-chain specific acyl-CoA dehydrogenase, mitochondrialAdd BLAST388

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27PhosphothreonineBy similarity1
Modified residuei51N6-acetyllysine; alternateBy similarity1
Modified residuei51N6-succinyllysine; alternateBy similarity1
Modified residuei72N6-acetyllysineBy similarity1
Modified residuei129N6-acetyllysine; alternateBy similarity1
Modified residuei129N6-succinyllysine; alternateBy similarity1
Modified residuei208N6-acetyllysineBy similarity1
Modified residuei262N6-acetyllysine; alternateBy similarity1
Modified residuei262N6-succinyllysine; alternateBy similarity1
Modified residuei292N6-acetyllysineBy similarity1
Modified residuei306N6-acetyllysine; alternateBy similarity1
Modified residuei306N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP15651
PRIDEiP15651

PTM databases

CarbonylDBiP15651
iPTMnetiP15651
PhosphoSitePlusiP15651

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

IntActiP15651, 1 interactor
STRINGi10116.ENSRNOP00000001556

Structurei

Secondary structure

1412
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 52Combined sources17
Turni53 – 56Combined sources4
Helixi57 – 63Combined sources7
Helixi68 – 77Combined sources10
Turni78 – 80Combined sources3
Beta strandi81 – 84Combined sources4
Helixi86 – 88Combined sources3
Helixi95 – 108Combined sources14
Helixi110 – 121Combined sources12
Helixi124 – 130Combined sources7
Helixi133 – 139Combined sources7
Helixi141 – 143Combined sources3
Beta strandi144 – 147Combined sources4
Beta strandi150 – 153Combined sources4
Beta strandi159 – 162Combined sources4
Beta strandi169 – 172Combined sources4
Beta strandi174 – 187Combined sources14
Turni188 – 191Combined sources4
Beta strandi193 – 201Combined sources9
Helixi203 – 208Combined sources6
Beta strandi209 – 218Combined sources10
Beta strandi222 – 224Combined sources3
Beta strandi230 – 232Combined sources3
Beta strandi238 – 249Combined sources12
Helixi250 – 252Combined sources3
Beta strandi253 – 256Combined sources4
Helixi260 – 296Combined sources37
Beta strandi298 – 303Combined sources6
Helixi304 – 306Combined sources3
Helixi308 – 336Combined sources29
Helixi342 – 367Combined sources26
Helixi368 – 371Combined sources4
Helixi378 – 385Combined sources8
Helixi386 – 389Combined sources4
Turni390 – 392Combined sources3
Helixi395 – 410Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JQIX-ray2.25A/B25-412[»]
ProteinModelPortaliP15651
SMRiP15651
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15651

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni269 – 272Substrate binding1 Publication4

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0139 Eukaryota
COG1960 LUCA
HOVERGENiHBG000224
InParanoidiP15651
KOiK00248

Family and domain databases

Gene3Di1.10.540.10, 1 hit
InterProiView protein in InterPro
IPR006089 Acyl-CoA_DH_CS
IPR006091 Acyl-CoA_Oxase/DH_cen-dom
IPR036250 AcylCo_DH-like_C
IPR009075 AcylCo_DH/oxidase_C
IPR013786 AcylCoA_DH/ox_N
IPR037069 AcylCoA_DH/ox_N_sf
IPR009100 AcylCoA_DH/oxidase_NM_dom
PfamiView protein in Pfam
PF00441 Acyl-CoA_dh_1, 1 hit
PF02770 Acyl-CoA_dh_M, 1 hit
PF02771 Acyl-CoA_dh_N, 1 hit
SUPFAMiSSF47203 SSF47203, 1 hit
SSF56645 SSF56645, 1 hit
PROSITEiView protein in PROSITE
PS00072 ACYL_COA_DH_1, 1 hit
PS00073 ACYL_COA_DH_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15651-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAALLARAG GSLGRALRAR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE
60 70 80 90 100
KELVPIAAQL DKEHLFPTSQ VKKMGELGLL AMDVPEELSG AGLDYLAYSI
110 120 130 140 150
ALEEISRGCA STGVIMSVNN SLYLGPILKF GSSQQKQQWI TPFTNGDKIG
160 170 180 190 200
CFALSEPGNG SDAGAASTTA REEGDSWVLN GTKAWITNSW EASATVVFAS
210 220 230 240 250
TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN LIFEDCRIPK
260 270 280 290 300
ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRHAF
310 320 330 340 350
GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMAKL
360 370 380 390 400
AASEAATAIS HQAIQILGGM GYVTEMPAER YYRDARITEI YEGTSEIQRL
410
VIAGHLLRSY RS
Length:412
Mass (Da):44,765
Last modified:November 1, 1995 - v2
Checksum:i3E4A052FC99B8E14
GO

Sequence cautioni

The sequence AAA40669 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05030 mRNA Translation: AAA40669.1 Different initiation.
PIRiB34252
RefSeqiNP_071957.1, NM_022512.2
UniGeneiRn.1167

Genome annotation databases

GeneIDi64304
KEGGirno:64304
UCSCiRGD:620514 rat

Similar proteinsi

Entry informationi

Entry nameiACADS_RAT
AccessioniPrimary (citable) accession number: P15651
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 163 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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